Journal
JOURNAL OF VIROLOGY
Volume 80, Issue 16, Pages 7918-7928Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00645-06
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Funding
- NCRR NIH HHS [RR17573, P41 RR017573] Funding Source: Medline
- NIAID NIH HHS [AI-065359, AI-43103, R01 AI025913, T32 AI007354, AI-25913, U54 AI065359, AI-07354] Funding Source: Medline
- NIGMS NIH HHS [GM-066087, R01 GM066087] Funding Source: Medline
- NINDS NIH HHS [T32 NS041219, NS-41219] Funding Source: Medline
- PHS HHS [266200400058C] Funding Source: Medline
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Coronavirus particles are enveloped and pleomorphic and are thus refractory to crystallization and symmetry-assisted reconstruction. A novel methodology of single-particle image analysis was applied to selected virus features to obtain a detailed model of the oligomeric state and spatial relationships among viral structural proteins. Two-dimensional images of the S, M, and N structural proteins of severe acute respiratory syndrome coronavirus and two other coronaviruses were refined to a resolution of similar to 4 nm. Proteins near the viral membrane were arranged in overlapping lattices surrounding a disordered core. Trimeric glycoprotein spikes were in register with four underlying ribonucleoprotein densities. However, the spikes were dispensable for ribonucleoprotein lattice formation. The ribonucleoprotein particles displayed coiled shapes when released from the viral membrane. Our results contribute to the understanding of the assembly pathway used by coronaviruses and other pleomorphic viruses and provide the first detailed view of coronavirus ultrastructure.
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